Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain.

@article{Valverde1994MolecularCA,
  title={Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain.},
  author={Angela M Valverde and James Sinnett-Smith and Johan Van Lint and Enrique 4 Rozengurt},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 18},
  pages={8572-6}
}
A serine/threonine protein kinase that binds phorbol esters and diacylglycerol (named protein kinase D, PKD) has been identified. PKD contains membrane localization signals and a cysteine-rich repeat sequence homologous to that seen in the regulatory domain of protein kinase C (PKC). A bacterially expressed N-terminal domain of PKD exhibited high-affinity phorbol ester binding activity (Kd = 35 nM). The diacylglycerol analog 1-oleoyl-2-acetylglycerol inhibited phorbol ester binding in a dose… CONTINUE READING
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